Recombinant Human ELFN2 Fc Chimera Protein, CF

When Recombinant Human mGluR7 Protein (9530-UR) is coated at 1 μg/mL, 100 μL/well, Recombinant Human ELFN2 Fc Chimera binds with an ED50 of 0.15-0.75 μg/mL.

2 μg/lane of Recombinant Human ELFN2 Fc Chimera Protein (Catalog # 10643-EF) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 97-112 kDa and 194-224 kDa, respectively.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human ELFN2 Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human mGluR7 Protein (Catalog # 9530-UR) is coated at 1 μg/mL, 100 μL/well, Recombinant Human ELFN2 Fc Chimera binds with an ED₅₀ of 0.15-0.75 μg/mL.
• Source: Human embryonic kidney cell, HEK293-derived human ELFN2 protein
  

  Human ELFN2 (Asp23-Tyr397) Accession # Q5R3F8.1	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus		C-terminus

• Accession #: Q5R3F8.1
• N-terminal Sequence: Asp23
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 69 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 97-112 kDa, under reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.
• Purity: >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human ELFN2 Fc Chimera Protein, CF

• dJ63G5.3 (putative Leucine rich protein)
• dJ63G5.3
• ELFN2
• extracellular leucine-rich repeat and fibronectin type III containing 2
• extracellular leucine-rich repeat and fibronectin type III domain containing 2
• extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2
• KIAA1904
• leucine rich repeat containing 62
• leucine-rich repeat and fibronectin type-III domain-containing protein 6
• leucine-rich repeat-containing protein 62
• LRRC62
• PPP1R29
• protein phosphatase 1, regulatory subunit 29

Background

Extracellular leucine-rich repeat and fibronectin type III domain-containing protein 2 (ELFN2), also known as protein phosphatase 1 regulatory subunit 29 (PPP1R29), is a member of the extracellular leucine-rich repeat (LRR) superfamily (1). Human ELFN2 consists of an extracellular domain (ECD) containing five LRR domains, one LRR C-terminal (LRRCT) domain and an FN3 domain, a transmembrane domain, and a cytoplasmic domain. Within the mature ECD, human ELFN2 shares 98% amino acid sequence identity with mouse and rat ELFN2. ELFN-2 is quite restricted to the nervous system in which it is broadly expressed in the cortex,  presumed glutamatergic neurons, hippocampus, pyramidal and granule cells, and in the striatum. It has been proposed that ELFN-2 could provide the requisite specificity of cellular interactions to mediate a large number of selective connectivity decisions thereby involved in neurite outgrowth, axon guidance, fasciculation, and synapse formation (2). ELFN2 has been identified as a novel postsynaptic adhesion molecule expressed throughout the brain (3). Mutations of ELFN2 have been reported in pancreatic cancer radiation resistance (4) and stress fracture (5).

1. Liu, C. et al. (2018) Mol. Ther. 26:2267.
2. Dolan, J. et al. (2007) BMC Genomics 8:320.
3. Dunn, H.A. et al. (2019) Mol. Psychiatry 24:1902.
4. Friedman E. et al. (2014) Genet. Res. (Camb) 96:e004.
5. Souchek L.L. et al. (2014) Br. J. Cancer 111:1139.

Bioinformatics

• Uniprot:
  • Q5R3F8.1()